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pubmed:abstractText |
C2 toxin elaborated by Clostridium botulinum type C is composed of two dissimilar protein components, designated components I and II. Component I of the toxin caused ADP-ribosylation of a protein of Mr 45,000 in chicken tissue homogenates and also purified nonmuscle but not muscle actin. The endogenous ADP-ribosylation of intracellular actin with C2 toxin was correlated with the morphological change in intact culture cells caused by the toxin. These results indicate that the biological activity of the toxin involves a novel enzymatic activity of component I, which catalyzes the preferential ADP-ribosylation of nonmuscle actin of the target cells.
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